title: Prelamin A is involved in early steps of muscle differentiation.
abstract: Lamin A is a nuclear lamina constituent implicated in a number of human disorders including Emery-Dreifuss muscular dystrophy. Since increasing evidence suggests a role of the lamin A precursor in nuclear functions, we investigated the processing of prelamin A during differentiation of C2C12 mouse myoblasts. We show that both protein levels and cellular localization of prelamin A are modulated during myoblast activation. Similar changes of lamin A-binding proteins emerin and LAP2alpha were observed. Furthermore, prelamin A was found in a complex with LAP2alpha in differentiating myoblasts. Prelamin A accumulation in cycling myoblasts by expressing unprocessable mutants affected LAP2alpha and PCNA amount and increased caveolin 3 mRNA and protein levels, while accumulation of prelamin A in differentiated muscle cells following treatment with a farnesyl transferase inhibitor appeared to inhibit caveolin 3 expression. Our data provide evidence for a critical role of the lamin A precursor in the early steps of muscle cell differentiation.
authors.affiliation: IGM-CNR, Unit of Bologna, c/o IOR, Via di Barbiano 1/10 I-40136 Bologna, Italy.
authors.forename: Cristina
authors.initials: C
authors.lastname: Capanni
authors.forename: Rosalba
authors.initials: R
authors.lastname: Del Coco
authors.forename: Stefano
authors.initials: S
authors.lastname: Squarzoni
authors.forename: Marta
authors.initials: M
authors.lastname: Columbaro
authors.forename: Elisabetta
authors.initials: E
authors.lastname: Mattioli
authors.forename: Daria
authors.initials: D
authors.lastname: Camozzi
authors.forename: Anna
authors.initials: A
authors.lastname: Rocchi
authors.forename: Katia
authors.initials: K
authors.lastname: Scotlandi
authors.forename: Nadir
authors.initials: N
authors.lastname: Maraldi
authors.forename: Roland
authors.initials: R
authors.lastname: Foisner
authors.forename: Giovanna
authors.initials: G
authors.lastname: Lattanzi
mesh_terms: D000818:Animals; D051244:Caveolin 3 / Q000235:genetics / Q000378:metabolism; D002454:Cell Differentiation / Q000235:genetics*; D002478:Cells, Cultured; D004268:DNA-Binding Proteins / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental; D006801:Humans; D034904:Lamin Type A; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D024510:Muscle Development / Q000235:genetics*; D018482:Muscle, Skeletal / Q000378:metabolism / Q000502:physiology; D032446:Myoblasts / Q000378:metabolism / Q000502:physiology; D009687:Nuclear Proteins / Q000378:metabolism / Q000502:physiology*; D011485:Protein Binding; D011498:Protein Precursors / Q000378:metabolism / Q000502:physiology*; D011499:Protein Processing, Post-Translational / Q000502:physiology; D013997:Time Factors
chemical_list: D051244:Caveolin 3; D004268:DNA-Binding Proteins; D034904:Lamin Type A; D008565:Membrane Proteins; D009687:Nuclear Proteins; D011498:Protein Precursors; C093413:lamina-associated polypeptide 2; C090764:prelamin A